S Phase Activation of the Histone H2B Promoter by OCA-S, a Coactivator Complex that Contains GAPDH as a Key Component

Zheng, Lei; Roeder, Robert G.; Luo, Yan

doi:10.1016/s0092-8674(03)00552-x

Cited by 488 publications

(468 citation statements)

References 33 publications

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“…Interestingly, it is clear now that GAPDH displays a distinct membrane, cytosolic and nuclear localization. In those subcellular sites, it is involved in a number of cellular functions, including endocytosis and membrane fusion (Glaser and Gross, 1995;Robbins et al, 1995), vesicular secretory transport (Tisdale, 2001), translational control (Yi et al, 2000), nuclear tRNA transport (Singh and Green, 1993), DNA replication (Zheng et al, 2003) and DNA repair (Krynetski et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…These include the transcriptional regulation of histone gene expression (Zheng et al, 2003), the role of GAPDH in nuclear membrane fusion (Nakagawa et al, 2003), in the modulation of telomere structure (Sundararaj et al, 2004), in the recognition of fraudulent nucleotides in DNA arising from cancer chemotherapy (Krynetski et al, 2003) and in triggering apoptosis (Chuang et al, 2005;Hara et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

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Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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We report here that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts in vitro and in vivo with the protein SET. This interaction is performed through the acidic domain of SET located at the carboxy terminal region. On analysing the functional relevance of SET-GAPDH interaction, we observed that GAPDH reverses in a dose-dependent manner, the inhibition of cyclin Bcdk1 activity produced by SET. Similarly to SET, GAPDH associates with cyclin B, suggesting that the regulation of cyclin B-cdk1 activity might be mediated not only by the interaction of GAPDH with SET but also with cyclin B. To analyse the putative role of GAPDH on cell cycle progression, HCT116 cells were transfected with a GAPDH expression vector. Results indicate that overexpression of GAPDH does not affect the timing of DNA replication but induces an increase in the number of mitosis, an advancement of the peak of cyclin B-cdk1 activity and an acceleration of cell cycle progression. All these results suggest that GAPDH might be involved in cell cycle regulation by modulating cyclin B-cdk1 activity.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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“…The much greater decrease in GAPDH elicited by VPA in the ChIP complex than in the nuclear preparation of unstimulated CGC ( Figure 6 vs Figure 5b) suggests that only a small fraction of nuclear GAPDH is present with histone proteins in the ChIP complex. Interestingly, it was recently reported that the histone H2B promoter interacts with a GAPDHcontaining transcriptional coactivator complex, 31 indicating that nuclear GAPDH may have an important function in gene transcription. GAPDH also selectively interacts with the polyglutamate region of huntingtin, 32 a Huntington's disease protein that accumulates in the nuclei as the pathophysiology progresses.…”

Section: Discussionmentioning

confidence: 99%

Valproic acid inhibits histone deacetylase activity and suppresses excitotoxicity-induced GAPDH nuclear accumulation and apoptotic death in neurons

et al. 2004

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Valproic acid (VPA), used to treat bipolar mood disorder and seizures, also inhibits histone deacetylase (HDAC). Here, we found that VPA and other HDAC inhibitors, butyrate and trichostatin A, robustly protected mature cerebellar granule cell cultures from excitotoxicity induced by SYM 2081 ((2S, 4R)-4-methylglutamate), an inhibitor of excitatory amino-acid transporters and an agonist of low-affinity kainate receptors. These neuroprotective effects required protracted treatment and were correlated with enhanced acetylated histone levels, indicating HDAC inhibition. SYM-induced excitotoxicity was blocked by MK-801 ((5R,10S)-( þ )-5-methyl-10,11-dihydro-5H-dibenzo[a,d]-cyclohepten-5,10-imine hydrogen maleate), supporting that the toxicity was largely N-methyl-D-aspartate receptor dependent. SYM excitotoxicity had apoptotic characteristics and was prevented by a caspase inhibitor. SYMinduced apoptosis was associated with a rapid and robust nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a housekeeping gene previously shown to be proapoptotic. VPA pretreatment suppressed SYM 2081-induced GAPDH nuclear accumulation, concurrent with its neuroprotective effects. Chromatin immunoprecipitation (ChIP) revealed that GAPDH is copresent with acetylated histone H3, including Lys9-acetylated histone, and that VPA treatment caused a time-dependent decrease in the levels of nuclear GAPDH with a concomitant increase in acetylated histones in the ChIP complex. Our results strongly suggest that VPA protects neurons from excitotoxicity through inhibition of HDAC activity and that this protective effect may involve suppression of excitotoxicity-induced accumulation of GAPDH protein in the nucleus.

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“…Mitogen-and stress-activated protein kinase-1 (MSK1) can be directly activated by p38 and ERK, and may mediate activation of CREB [62][63][64]. p38 is also thought to regulate S phase activation of histone 2B (H2B) promoter through OCA-S, a component of p38 [65].…”

Section: Downstream Substrates Of P38 Group Map Kinases Protein Kinasmentioning

confidence: 99%

Activation and signaling of the p38 MAP kinase pathway

2005

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The family members of the mitogen-activated protein (MAP) kinases mediate a wide variety of cellular behaviors in response to extracellular stimuli. One of the four main sub-groups, the p38 group of MAP kinases, serve as a nexus for signal transduction and play a vital role in numerous biological processes. In this review, we highlight the known characteristics and components of the p38 pathway along with the mechanism and consequences of p38 activation. We focus on the role of p38 as a signal transduction mediator and examine the evidence linking p38 to inflammation, cell cycle, cell death, development, cell differentiation, senescence and tumorigenesis in specific cell types. Upstream and downstream components of p38 are described and questions remaining to be answered are posed. Finally, we propose several directions for future research on p38.

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S Phase Activation of the Histone H2B Promoter by OCA-S, a Coactivator Complex that Contains GAPDH as a Key Component

Cited by 488 publications

References 33 publications

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Valproic acid inhibits histone deacetylase activity and suppresses excitotoxicity-induced GAPDH nuclear accumulation and apoptotic death in neurons

Activation and signaling of the p38 MAP kinase pathway

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